The voltage-dependent anion selective channel 1 (VDAC1) topography in the mitochondrial outer membrane as detected in intact cell

Voltage-Dependent Anion selective Channel maintains the permeability of the outer mitochondrial membrane and is relevant in bioenergetic metabolism and apoptosis. The structure of the protein was shown to be a β-barrel formed by 19 strands. The topology or sideness of the pore has been predicted wit...

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Bibliographic Details
Published in:PloS one 2013-12, Vol.8 (12), p.e81522-e81522
Main Authors: Tomasello, Marianna F, Guarino, Francesca, Reina, Simona, Messina, Angela, De Pinto, Vito
Format: Article
Language:English
Subjects:
Anions
Apoptosis
Bcl-2 protein
C-Terminus
Caspase
Caspases - metabolism
Electric potential
Environmental science
Experiments
Geology
HeLa Cells
Hexokinase
Humans
Membrane permeability
Metabolism
Mitochondria
Mitochondria - drug effects
Mitochondria - metabolism
Mitochondrial Membranes - drug effects
Mitochondrial Membranes - metabolism
Molecular biology
Oligopeptides - metabolism
Peptide Hydrolases - metabolism
Permeability
Physiological aspects
Protein Binding - drug effects
Protein structure
Protein Transport - drug effects
Proteins
Recombinant Fusion Proteins - metabolism
Staurosporine - pharmacology
Topography
Topology
Voltage
Voltage-Dependent Anion Channel 1 - chemistry
Voltage-Dependent Anion Channel 1 - metabolism
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Summary:Voltage-Dependent Anion selective Channel maintains the permeability of the outer mitochondrial membrane and is relevant in bioenergetic metabolism and apoptosis. The structure of the protein was shown to be a β-barrel formed by 19 strands. The topology or sideness of the pore has been predicted with various approaches but a general consensus was never reached. This is an important issue since VDAC is considered receptor of Hexokinase and Bcl-2. We fused at VDAC1 C-terminus two tags separated by a caspase cleavage site. Activation in cellulo of caspases was used to eventually separate the two reporters. This experiment did not require the isolation of mitochondria and limited the possibility of outer membrane rupture due to similar procedures. Our results show that the C-terminus end of VDAC faces the mitochondrial inter-membrane space.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0081522